Define Michaelis constant of an enzyme. -Biology

Define Michaelis constant of an enzyme. -Biology
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Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these

Description : Substrate concentration at which an enzyme attains half its maximum velocity is (A) Threshold value (B) Michaelis-Menton constant (C) Concentration level (D) None of these

Last Answer : Answer : B

The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Description : The Michaelis constant, Km is (A) Numerically equal to ½ Vmax (B) Dependent on the enzyme concentration (C) Independent of pH (D) Numerically equal to the substrate concentration that gives half maximal velocity

Last Answer : Answer : D

Different isoenzymes of an enzyme have the same (A) Amino acid sequence (B) Michaelis constant (C) Catalytic activity (D) All of these

Description : Different isoenzymes of an enzyme have the same (A) Amino acid sequence (B) Michaelis constant (C) Catalytic activity (D) All of these

Last Answer : Answer : C

Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Description : Kinetics of an allosteric enzyme are explained by (A) Michaelis-Menten equation (B) Lineweaver-Burk plot (C) Hill plot (D) All of these

Last Answer : Answer : C

Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein

Description : Michaelis – Menten equation is used to explain the effect of substrate concentration on (A) Carbohydrate (B) Enzyme (C) Lipid (D) Protein

Last Answer : Answer : B

........................ studied the kinetics of enzyme catalysis. a. Arrhenius b. Rutherford c. Micheal Faraday d. Michaelis & Menten

Description : ........................ studied the kinetics of enzyme catalysis. a. Arrhenius b. Rutherford c. Micheal Faraday d. Michaelis & Menten

Last Answer : d. Michaelis & Menten

What is Michaelis Menten constant? -Biology

Description : What is Michaelis Menten constant? -Biology

Last Answer : answer:

Does Sebastian Michaelis have a brother?

Description : Does Sebastian Michaelis have a brother?

Last Answer : no

Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Description : Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding

Last Answer : Answer : C

A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition

Description : A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V) may indicate (A) Michaelis-Menten kinetics (B) Co-operative binding (C) Competitive inhibition (D) Non-competitive inhibition

Last Answer : Answer : B

From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S

Description : From the L ineweaver-Burk p lot of Michaelis-Menten equation, Km and Vmax can be determined when V is the reaction velocity at substrate concentration S, the X-axis experimental data are expressed as (A) 1/V (B) V (C) 1/S (D) S

Last Answer : Answer : C

The phenomenon of inhibition of glycolysis by O2 is termed as (A) Red drop (B) Pasteur effect (C) Michaelis effect (D) Fischer’s effect

Description : The phenomenon of inhibition of glycolysis by O2 is termed as (A) Red drop (B) Pasteur effect (C) Michaelis effect (D) Fischer’s effect

Last Answer : Answer : B

What is Michaelis-Menten Theory ?

Description : What is Michaelis-Menten Theory ?

Last Answer : It is otherwise called enzyme-substrate complex theory. The enzyme combines with the substrate, to form an enzyme-substrate complex, which immediately breaks down to the enzyme and the product.

The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be described as (A) Independent of enzyme concentration (B) A constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Description : The rate of an enzyme catalyzed reaction was measured using several substrate concentrations that were much lower than Km, the dependence of reaction velocity on substrate concentration can best be ... constant fraction of Vmax (C) Equal to Km (D) Proportional to the substrate concentration

Last Answer : Answer : C

In enzyme assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature

Description : In enzyme assays, all the following are kept constant except (A) Substrate concentration (B) Enzyme concentration (C) pH (D) Temperature

Last Answer : Answer : B

In enzyme kinetics Km implies (A) The substrate concentration that gives one half Vmax (B) The dissocation constant for the enzyme substrate comples (C) Concentration of enzyme (D) Half of the substrate concentration required to achieve Vmax

Description : In enzyme kinetics Km implies (A) The substrate concentration that gives one half Vmax (B) The dissocation constant for the enzyme substrate comples (C) Concentration of enzyme (D) Half of the substrate concentration required to achieve Vmax

Last Answer : Answer : A

Main function of an enzyme is to A- increase the activation energy B- decrease the activation energy C- maintain constant activation energy D- .none of these

Description : Main function of an enzyme is to A- increase the activation energy B- decrease the activation energy C- maintain constant activation energy D- .none of these

Last Answer : decrease the activation energy

Which one of the following statements regarding a catalyst is not correct? A An enzyme is a catalyst that only binds certain substrates. B An enzyme is a protein that is a highly efficient catalyst for one or more chemical reactions in a living system. C Catalysts increase the rate of a reaction by altering the mechanism, thereby increasing the activation energy. D Catalysts do not alter the equilibrium constant for a chemical reaction.

Description : Which one of the following statements regarding a catalyst is not correct? A An enzyme is a catalyst that only binds certain substrates. B An enzyme is a protein that is a highly ... increasing the activation energy. D Catalysts do not alter the equilibrium constant for a chemical reaction.

Last Answer : C Catalysts increase the rate of a reaction by altering the mechanism, thereby increasing the activation energy.